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A solenoid design for assessing determinants of parallel ?-sheet registration.

ABSTRACT: A novel protein construct is presented that combines a homotrimeric, triple-stranded ?-helix as a guest to a homotrimeric foldon unit from bacteriophage T4 fibritin. The ?-helical solenoid selected is short (46 residues) and is part of a subdomain of the T4 cell-puncturing device. The resultant design is trimeric and displays greatly enhanced stability over each sub-component alone. The intended goal is a design that will enable evaluation of sequence determinants that promote in-register versus out-of-register parallel ?-sheet homotrimerization. Towards that end, the importance of a set of three buried salt-bridges was evaluated by converting them to residues otherwise consistently found throughout the natural solenoid at the same positions. The critical role of the charged residues in the salt-bridges was evident in that their elimination resulted in amyloid-like aggregation.

SUBMITTER: White EM

PROVIDER: S-EPMC4646161 | biostudies-literature | 2015 Dec

REPOSITORIES: biostudies-literature

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A solenoid design for assessing determinants of parallel β-sheet registration.

White Ellen M EM Miranker Andrew D AD

Protein engineering, design & selection : PEDS 20151020 12

A novel protein construct is presented that combines a homotrimeric, triple-stranded β-helix as a guest to a homotrimeric foldon unit from bacteriophage T4 fibritin. The β-helical solenoid selected is short (46 residues) and is part of a subdomain of the T4 cell-puncturing device. The resultant design is trimeric and displays greatly enhanced stability over each sub-component alone. The intended goal is a design that will enable evaluation of sequence determinants that promote in-register versus ...[more]

PMID: 26487712

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Project description:MOTIVATION: Solenoid proteins are emerging as a protein class with properties intermediate between structured and intrinsically unstructured proteins. Containing repeating structural units, solenoid proteins are expected to share sequence similarities. However, in many cases, the sequence similarities are weak and non-detectable. Moreover, solenoids can be degenerated and widely vary in the number of units. So that it is difficult to detect them. Recently, several solenoid repeats detection methods have been proposed, such as self-alignment of the sequence, spectral analysis and discrete Fourier transform of sequence. Although these methods have shown good performance on certain data sets, they often fail to detect repeats with weak similarities. In this article, we propose a new approach to recognize solenoid repeats and non-solenoid proteins using stationary wavelet packet transform (SWPT). Our method associates with three advantages: (i) naturally representing five main factors of protein structure and properties by wavelet analysis technique; (ii) extracting novel wavelet features that can capture hidden components from solenoid sequence similarities and distinguish them from global proteins; (iii) obtaining statistics features that capture repeating motifs of solenoid proteins. RESULTS: Our method analyzes the characteristics of amino acid sequence in both spectral and temporal domains using SWPT. Both global and local information of proteins are captured by SWPT coefficients. We obtain and integrate wavelet-based features and statistics-based features of amino acid sequence to improve the classification task. Our proposed method is evaluated by comparing to state-of-the-art methods such as HHrepID and REPETITA. The experimental results show that our algorithm consistently outperforms them in areas under ROC curve. At the same false positive rate, the sensitivity of our WAVELET method is higher than other methods. AVAILABILITY: http://www.naaan.org/anvo/Software/Software.htm.

Dataset Information

A solenoid design for assessing determinants of parallel ?-sheet registration.

Publications

A solenoid design for assessing determinants of parallel β-sheet registration.

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